2vtg: Difference between revisions

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{{Seed}}
[[Image:2vtg.jpg|left|200px]]


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==Crystal Structure of Human Iba2, trigonal crystal form==
The line below this paragraph, containing "STRUCTURE_2vtg", creates the "Structure Box" on the page.
<StructureSection load='2vtg' size='340' side='right'caption='[[2vtg]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2vtg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VTG FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_2vtg|  PDB=2vtg  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vtg OCA], [https://pdbe.org/2vtg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vtg RCSB], [https://www.ebi.ac.uk/pdbsum/2vtg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vtg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AIF1L_HUMAN AIF1L_HUMAN] Actin-binding protein that promotes actin bundling. May neither bind calcium nor depend on calcium for function.<ref>PMID:18699778</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vt/2vtg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vtg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Iba2 is a homolog of ionized calcium-binding adapter molecule 1 (Iba1), a 17-kDa protein that binds and cross-links filamentous actin (F-actin) and localizes to membrane ruffles and phagocytic cups. Here, we present the crystal structure of human Iba2 and its homodimerization properties, F-actin cross-linking activity, cellular localization and recruitment upon bacterial invasion in comparison with Iba1. The Iba2 structure comprises two central EF-hand motifs lacking bound Ca2+. Iba2 crystallized as a homodimer stabilized by a disulfide bridge and zinc ions. Analytical ultracentrifugation revealed a different mode of dimerization under reducing conditions that was independent of Ca2+. Furthermore, no binding of Ca2+ up to 0.1 mM was detected by equilibrium dialysis. Correspondingly, Iba EF-hand motifs lack residues essential for strong Ca2+ coordination. Sedimentation experiments and microscopy detected pronounced, indistinguishable F-actin binding and cross-linking activity of Iba1 and Iba2 with induction of F-actin bundles. Fluorescent Iba fusion proteins were expressed in HeLa cells and co-localized with F-actin. Iba1 was recruited into cellular projections to a larger extent than Iba2. Additionally, we studied Iba recruitment in a Shigella invasion model that induces cytoskeletal rearrangements. Both proteins were recruited into the bacterial invasion zone and Iba1 was again concentrated slightly higher in the cellular extensions.


===CRYSTAL STRUCTURE OF HUMAN IBA2, TRIGONAL CRYSTAL FORM===
Structural and functional characterization of human Iba proteins.,Schulze JO, Quedenau C, Roske Y, Adam T, Schuler H, Behlke J, Turnbull AP, Sievert V, Scheich C, Mueller U, Heinemann U, Bussow K FEBS J. 2008 Sep;275(18):4627-40. Epub 2008 Aug 11. PMID:18699778<ref>PMID:18699778</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 18699778 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_18699778}}
__TOC__
 
</StructureSection>
==About this Structure==
2VTG is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VTG OCA].
 
==Reference==
<ref group="xtra">PMID:18699778</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Buessow, K.]]
[[Category: Large Structures]]
[[Category: Heinemann, U.]]
[[Category: Buessow K]]
[[Category: Mueller, U.]]
[[Category: Heinemann U]]
[[Category: Quedenau, C.]]
[[Category: Mueller U]]
[[Category: Roske, Y.]]
[[Category: Quedenau C]]
[[Category: Schulze, J O.]]
[[Category: Roske Y]]
[[Category: Turnbull, A.]]
[[Category: Schulze JO]]
[[Category: Actin crosslinking]]
[[Category: Turnbull A]]
[[Category: Calcium binding]]
[[Category: Ef-hand]]
[[Category: Ionized calcium binding adapter molecule 2]]
[[Category: Metal-binding protein]]
 
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Retrieved from "https://proteopedia.org/2vtg"